Evidence map›Paper›PMID 24752014›Full record

ReviewNature reviews. Nephrology2014

Proteostasis in endoplasmic reticulum--new mechanisms in kidney disease.

Reiko Inagi, Yu Ishimoto, Masaomi Nangaku

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Nephrology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing papers in PubMed
8.7field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

121 citing papers in PubMed, 214 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. GALNT3 in Ischemia-Reperfusion Injury of the Kidney.Journal of the American Society of Nephrology : JASN · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review

61 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Reiko InagiDivision of Chronic Kidney Disease Pathophysiology, The University of Tokyo Graduate School of Medicine, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8655, Japan.
Yu IshimotoDivision of Nephrology and Endocrinology, The University of Tokyo Graduate School of Medicine, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8655, Japan.
Masaomi NangakuDivision of Nephrology and Endocrinology, The University of Tokyo Graduate School of Medicine, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8655, Japan.
The University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cells use an exquisite network of mechanisms to maintain the integrity and functionality of their protein components. In the endoplasmic reticulum (ER), these networks of protein homeostasis--referred to as proteostasis--regulate protein synthesis, folding and degradation via the unfolded protein response (UPR) pathway. The UPR pathway has two components: the adaptive UPR pathway, which predominantly maintains the ER function or ER proteostasis, and the apoptotic UPR pathway, which eliminates dysfunctional cells that have been subject to long-term or severe ER stress. Dysregulation of the UPR pathway often occurs in glomerular or tubulointerstitial cells under a pathogenic microenvironment, such as oxidative stress, glycative stress or hypoxia. A defective UPR is highly deleterious to renal cell function and viability and is thereby implicated in the pathophysiology of various kidney diseases. Accumulating evidence provides a link between the UPR pathway and mitochondrial structure and function, indicating the important role of ER proteostasis in the maintenance of mitochondrial homeostasis. Restoration of normal proteostasis, therefore, holds promise in protecting the kidney from pathogenic stresses as well as ageing. This Review is focused on the role of the ER stress and UPR pathway in the maintenance of ER proteostasis, and highlights the involvement of the derangement of ER proteostasis and ER stress in various pathogenic stress signals in the kidney.

Indexed as

AnimalsApoptosisAutophagyEndoplasmic ReticulumHomeostasisHumansHypoxiaKidneyKidney DiseasesMolecular ChaperonesNephritisOxidative StressProteasome InhibitorsProteinsStress, PhysiologicalUnfolded Protein ResponseMolecular ChaperonesProteasome InhibitorsProteins

Identifiers

PMID24752014
OpenAlexW2005039062

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.